Conformational diversity of dynactin sidearm and domain organization of its subunit p150

Using nanogold labeling and deletion mutant analysis, we determined the domain organization of dynactin subunit p150 and discovered that its CC1 domain adopted either a folded or an extended form. Furthermore, the entire sidearm of dynactin exhibited several characteristic forms, and the equilibrium among them depended on salt concentrations.

Download Full-text

Deletion mutant analysis of the Staphylococcus aureus plasmid pI258 mercury-resistance determinant

Canadian Journal of Microbiology ◽

10.1139/m91-106 ◽

1991 ◽

Vol 37 (8) ◽

pp. 624-631 ◽

Cited By ~ 16

Author(s):

Kenneth Babich ◽

Mike Engle ◽

Jeffery S. Skinner ◽

Richard A. Laddaga

Keyword(s):

Staphylococcus Aureus ◽

Ion Transport ◽

Copy Number ◽

Deletion Mutant ◽

Resistance Determinant ◽

Mercury Resistance ◽

Mutant Analysis ◽

Mer Operon ◽

Copy Number Plasmid ◽

High Copy Number Plasmid

Deletion mutant analysis of the mercury-resistant determinant (mer operon) from the Staphylococcus aureus plasmid pI258 was used to verify the location of the merA and merB genes and to show the existence of mercuric ion transport gene(s). ORF5 was confirmed to be a transport gene and has an amino acid product sequence homologous to the merT gene products from several gram-negative bacteria and a Bacillus species. Deletion analysis established that inactivation of merA on a broad-spectrum mer resistance determinant resulted in a mercury-hypersensitive phenotype. Gene dosage had no apparent effect on the level of resistance conferred by the intact mer operon or on the expression of an inducible phenotype, except that when the intact pI258 mer operon was on a high copy number plasmid, uninduced cells possessed a volatilization rate that was at most only 3.5-fold less than that observed for induced cells. There was no need for mercury ion transport proteins for full resistance when the mer operon was expressed in a high copy number plasmid. Key words: mercury resistance, Staphylococcus aureus plasmid.

Download Full-text

Domain organization and conformational change of dynactin p150

10.1101/459040 ◽

2018 ◽

Author(s):

Kei Saito ◽

Takashi Murayama ◽

Tomone Hata ◽

Takuya Kobayashi ◽

Keitaro Shibata ◽

...

Keyword(s):

Electron Microscopy ◽

Conformational Change ◽

Coiled Coil ◽

Deletion Analysis ◽

Filamentous Structure ◽

Extended Form ◽

Domain Organization ◽

Structural Details ◽

Microtubule Motor ◽

Dynactin Complex

AbstractDynactin is a principal regulator of the minus-end directed microtubule motor dynein. The sidearm of dynactin is essential for binding to microtubules and regulation of dynein activity. Although our understanding of the structure of the dynactin backbone (Arp1 rod) has greatly improved recently, structural details of the sidearm part remain elusive. Here, electron microscopy of individual molecules of the dynactin complex revealed that the sidearm was highly flexible and exhibited diverse morphologies. Utilizing mutants for nanogold labeling and deletion analysis, we determined the domain organization of the largest subunit p150 and identified a filamentous structure protruding from the head domain of the sidearm as the coiled-coil 1 (CC1), the dynein-binding domain, in p150. Furthermore, the protrusion formed by CC1 exhibited either a folded or an extended form, suggesting that CC1 works as an extending “arm”. These findings provide clues to understand how dynactin binds to microtubules and regulates dynein.

Download Full-text

Localization of a DNA topoisomerase II to mitochondria inDictyostelium discoideum: Deletion mutant analysis and mitochondrial targeting signal presequence

Journal of Plant Research ◽

10.1007/bf02506844 ◽

1997 ◽

Vol 110 (1) ◽

pp. 65-75 ◽

Cited By ~ 5

Author(s):

Kayoko Komori ◽

Fumiaki Maruo ◽

Takahiro Morio ◽

Hideko Urushihara ◽

Yoshimasa Tanaka

Keyword(s):

Deletion Mutant ◽

Topoisomerase Ii ◽

Dna Topoisomerase Ii ◽

Mitochondrial Targeting ◽

Dna Topoisomerase ◽

Mutant Analysis ◽

Targeting Signal

Download Full-text

Marker-Assisted Molecular Profiling, Deletion Mutant Analysis, and RNA-Seq Reveal a Disease Resistance Cluster Associated with Uromyces appendiculatus Infection in Common Bean Phaseolus vulgaris L.

International Journal of Molecular Sciences ◽

10.3390/ijms18061109 ◽

2017 ◽

Vol 18 (6) ◽

pp. 1109 ◽

Cited By ~ 1

Author(s):

Antonette Todd ◽

Nicole Donofrio ◽

Venkateswara Sripathi ◽

Phillip McClean ◽

Rian Lee ◽

...

Keyword(s):

Disease Resistance ◽

Phaseolus Vulgaris ◽

Common Bean ◽

Deletion Mutant ◽

Molecular Profiling ◽

Uromyces Appendiculatus ◽

Rna Seq ◽

Phaseolus Vulgaris L ◽

Mutant Analysis

Download Full-text

Appendage-Mediated Surface Adherence of Sulfolobus solfataricus

Journal of Bacteriology ◽

10.1128/jb.01061-09 ◽

2009 ◽

Vol 192 (1) ◽

pp. 104-110 ◽

Cited By ~ 62

Author(s):

Behnam Zolghadr ◽

Andreas Klingl ◽

Andrea Koerdt ◽

Arnold J. M. Driessen ◽

Reinhard Rachel ◽

...

Keyword(s):

Biofilm Formation ◽

Deletion Mutant ◽

Sulfolobus Solfataricus ◽

Extracellular Polysaccharides ◽

Initial Attachment ◽

Mutant Analysis ◽

Carbon Coated

ABSTRACT Attachment of microorganisms to surfaces is a prerequisite for colonization and biofilm formation. The hyperthermophilic crenarchaeote Sulfolobus solfataricus was able to attach to a variety of surfaces, such as glass, mica, pyrite, and carbon-coated gold grids. Deletion mutant analysis showed that for initial attachment the presence of flagella and pili is essential. Attached cells produced extracellular polysaccharides containing mannose, galactose, and N-acetylglucosamine. Genes possibly involved in the production of the extracellular polysaccharides were identified.

Download Full-text